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Database: UniProt/TrEMBL
Entry: E8TLZ9_MESCW
LinkDB: E8TLZ9_MESCW
Original site: E8TLZ9_MESCW 
ID   E8TLZ9_MESCW            Unreviewed;       379 AA.
AC   E8TLZ9;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   28-FEB-2018, entry version 57.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   OrderedLocusNames=Mesci_1221 {ECO:0000313|EMBL:ADV10384.1};
OS   Mesorhizobium ciceri biovar biserrulae (strain HAMBI 2942 / LMG 23838
OS   / WSM1271).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=765698 {ECO:0000313|EMBL:ADV10384.1, ECO:0000313|Proteomes:UP000007471};
RN   [1] {ECO:0000313|Proteomes:UP000007471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAMBI 2942 / LMG 23838 / WSM1271
RC   {ECO:0000313|Proteomes:UP000007471};
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
RA   Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Nandasena K., Reeve W.G.,
RA   Howieson J.G., O'Hara G., Tiwari R.P., Woyke T.;
RT   "Complete sequence of chromosome of Mesorhizobium ciceri bv.
RT   biserrulae WSM1271.";
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. May also act on other amino acids. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
CC   -!- CATALYTIC ACTIVITY: L-alanine = D-alanine. {ECO:0000256|HAMAP-
CC       Rule:MF_01201, ECO:0000256|SAAS:SAAS00630646}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01201,
CC         ECO:0000256|PIRSR:PIRSR600821-50,
CC         ECO:0000256|SAAS:SAAS00758845};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-
CC       alanine from L-alanine: step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01201, ECO:0000256|SAAS:SAAS00630654}.
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DR   EMBL; CP002447; ADV10384.1; -; Genomic_DNA.
DR   RefSeq; WP_013529079.1; NC_014923.1.
DR   RefSeq; YP_004140434.1; NC_014923.1.
DR   ProteinModelPortal; E8TLZ9; -.
DR   STRING; 765698.Mesci_1221; -.
DR   EnsemblBacteria; ADV10384; ADV10384; Mesci_1221.
DR   GeneID; 10116669; -.
DR   KEGG; mci:Mesci_1221; -.
DR   PATRIC; fig|765698.3.peg.1655; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031445; -.
DR   KO; K01775; -.
DR   OMA; WRGPILL; -.
DR   OrthoDB; POG091H022F; -.
DR   BioCyc; MCIC765698:GHQ5-1219-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000007471; Chromosome.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.40.37.10; -; 1.
DR   Gene3D; 3.20.20.10; -; 1.
DR   HAMAP; MF_01201; Ala_racemase; 1.
DR   InterPro; IPR000821; Ala_racemase.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR011079; Ala_racemase_C.
DR   InterPro; IPR001608; Ala_racemase_N.
DR   InterPro; IPR020622; Ala_racemase_pyridoxalP-BS.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   Pfam; PF00842; Ala_racemase_C; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   PRINTS; PR00992; ALARACEMASE.
DR   SMART; SM01005; Ala_racemase_C; 1.
DR   SUPFAM; SSF50621; SSF50621; 1.
DR   SUPFAM; SSF51419; SSF51419; 1.
DR   TIGRFAMs; TIGR00492; alr; 1.
DR   PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000007471};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:ADV10384.1};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|PIRSR:PIRSR600821-50, ECO:0000256|SAAS:SAAS00722456};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007471}.
FT   DOMAIN      253    377       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     53     53       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    274    274       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     152    152       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     320    320       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      53     53       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   379 AA;  39938 MW;  025E8AFC3015C87B CRC64;
     MNDALQKSPP EEVTATSEVA AGAILTIDLG AIRENYRRLK ARLGDVACAG VLKADGYGLG
     AGQVGAALLR EGCDIFFVAL LGEGVALRRS LGAGPAIFVL NGIPPGAETD AVAANLCAVI
     NSPEQLAAWR SAARRAGRKL PAAVQVDSGM SRLGMAPRDV DRIAADPQAF DGIDIRYVMS
     HLACADEPEH PANEKQRSVF ERLRAMLPKA PASLTNSSGI FLGPSFHYDL ARPGAALYGI
     NPTPPKSNPM LPVVRLQAKV AQTRSVEKGA GVGYGHSYHA QGPLRLATIS FGYADGWQRR
     AASAAWFEGV RLPFVGRVSM DSIILDISAL PAGRLREGDL VELLGPSQSV DDAAGHAGTI
     GYEILTSLGP RFHRRYVGG
//
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